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Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus.

Abstract:

The majority of proteins exist in vivo within macromolecular assemblies whose functions are dependent on dynamical processes spanning a wide range of time scales. One such assembly is formed by the molecular chaperone αB-crystallin that exists in a variety of exchanging oligomeric states, centred on a mass of approximately 560 kDa. For many macromolecular assemblies, including αB-crystallin, the inherent dynamics, heterogeneity and high mass contribute to difficulties in quantitative studies....

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2011.07.017

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Journal:
Journal of molecular biology More from this journal
Volume:
413
Issue:
2
Pages:
310-320
Publication date:
2011-10-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Language:
English
Keywords:
Pubs id:
pubs:170198
UUID:
uuid:a1c3feeb-68c4-44f9-84dd-710014211876
Local pid:
pubs:170198
Source identifiers:
170198
Deposit date:
2013-11-16

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